Pcf11 is a subunit of an essential polyadenylation factor in Saccharomyces cerevisiae, CFIA. Pcf11 binds to Clp1, another subunit of CFIA whose interaction is responsible for maintaining a tight coupling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery [, ]. Pcf11 is a bifunctional protein involved in pre-mRNA 3' end processing and transcription termination [, ].

The C-terminal section of cleavage stimulation and termination factor CstF-64 (CSTF2) and its yeast orthologue Rna15 form a discreet structure that is crucial for mRNA 3'-end processing []. This domain interacts with Pcf11 and possibly PC4, thus linking CSTF2 to transcription, transcriptional termination, and cell growth [].Proteins containing this domain also include Pti1 protein from budding yeast. Pti1 is an essential component of CPF (cleavage and polyadenylation factor) involved in 3' end formation of snoRNA and mRNA [].

The C-terminal domain (CTD) of the large subunit of RNA polymerase II is aplatform for mRNA processing factors and links gene transcription to mRNAcapping, splicing and polyadenylation. CTD recognition is dependent on thephosphorylation state of the CTD itself, which varies during the course oftranscription but has also been linked to the isomerization state of the CTD'sproline residues. Several RNA-processing factors recognise the CTD by means ofa conserved CTD-interacting domain (CID). Factors with CID domains include theserine/arginine-rich-like factors SCAF4 and SCAF8, Nrd1 (which is implicatedin polyadenylation-independent RNA 3'-end formation) and Pcf11. Pcf11 is aconserved and essential subunit of the yeast cleavage factor 1A, which isrequired for 3'-RNA processing and transcription termination [, ].The CID domain is a right-handed superhelix of eight alpha-helices forming acompact domain. The CID fold closely resembles that of VHSdomains and is related to armadillo-repeat proteins , except for the two amino-terminal helices. Amino acid residuesin the hydrophobic core of the domain are highly conserved across CID domains[, ].

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